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P08148

- GP63_LEIMA

UniProt

P08148 - GP63_LEIMA

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Protein

Leishmanolysin

Gene

gp63

Organism
Leishmania major
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Has an integral role during the infection of macrophages in the mammalian host.

Catalytic activityi

Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi264 – 2641Zinc; catalytic
Active sitei265 – 2651
Metal bindingi268 – 2681Zinc; catalytic
Metal bindingi334 – 3341Zinc; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Leishmanolysin (EC:3.4.24.36)
Alternative name(s):
Cell surface protease
Major surface glycoprotein
Major surface protease
Promastigote surface endopeptidase
Protein gp63
Gene namesi
Name:gp63
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi254 – 2541Y → D: No significant effect on protein expression levels or catalytic activity. 1 Publication
Mutagenesisi264 – 2641H → F or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
Mutagenesisi265 – 2651E → D: No significant effect on protein expression levels but almost abolishes catalytic activity. 1 Publication
Mutagenesisi268 – 2681H → N or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
Mutagenesisi300 – 3001N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi407 – 4071N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi534 – 5341N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi577 – 5771N → L: Causes extracellular release of the protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence AnalysisAdd
BLAST
Propeptidei40 – 10061Activation peptide1 PublicationPRO_0000028667Add
BLAST
Chaini101 – 577477LeishmanolysinPRO_0000028668Add
BLAST
Propeptidei578 – 60225Removed in mature formPRO_0000028669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi125 ↔ 1421 Publication
Disulfide bondi191 ↔ 2301 Publication
Glycosylationi300 – 3001N-linked (GlcNAc...)2 Publications
Disulfide bondi314 ↔ 3861 Publication
Disulfide bondi393 ↔ 4551 Publication
Disulfide bondi406 ↔ 4251 Publication
Glycosylationi407 – 4071N-linked (GlcNAc...)2 Publications
Disulfide bondi415 ↔ 4891 Publication
Disulfide bondi466 ↔ 5101 Publication
Disulfide bondi515 ↔ 5651 Publication
Glycosylationi534 – 5341N-linked (GlcNAc...)1 Publication
Disulfide bondi535 ↔ 5581 Publication
Lipidationi577 – 5771GPI-anchor amidated asparagine1 Publication

Post-translational modificationi

The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

PTM databases

UniCarbKBiP08148.

Miscellaneous databases

PMAP-CutDBP08148.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1144
Helixi116 – 1194
Beta strandi131 – 1333
Beta strandi135 – 1373
Beta strandi139 – 1413
Helixi144 – 1463
Helixi150 – 1589
Helixi160 – 16910
Beta strandi172 – 1743
Beta strandi177 – 1815
Helixi191 – 1933
Helixi198 – 2025
Beta strandi205 – 2073
Beta strandi209 – 2157
Beta strandi226 – 2327
Beta strandi238 – 2447
Helixi247 – 2493
Helixi256 – 26914
Helixi274 – 2796
Beta strandi283 – 2875
Helixi289 – 2913
Beta strandi296 – 2994
Helixi302 – 31211
Beta strandi320 – 3223
Turni328 – 3325
Beta strandi333 – 3353
Turni337 – 3393
Beta strandi346 – 3483
Helixi356 – 3649
Helixi372 – 3743
Turni380 – 3834
Helixi386 – 3905
Beta strandi393 – 3953
Beta strandi398 – 4003
Turni402 – 4043
Beta strandi420 – 4256
Helixi435 – 4373
Beta strandi440 – 4423
Turni450 – 4545
Beta strandi458 – 4658
Helixi470 – 4723
Turni475 – 4773
Helixi478 – 4803
Beta strandi487 – 4948
Beta strandi506 – 51611
Turni517 – 5204
Beta strandi521 – 5255
Beta strandi540 – 5423
Helixi543 – 5453
Beta strandi548 – 5503
Beta strandi555 – 5573
Helixi561 – 5655
Helixi569 – 5724

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LMLX-ray1.86A100-577[»]
ProteinModelPortaliP08148.
SMRiP08148. Positions 100-574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08148.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08148-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH
60 70 80 90 100
DAMQARVRQS VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV
110 120 130 140 150
VRDVNWGALR IAVSTEDLTD PAYHCARVGQ HVKDHAGAIV TCTAEDILTN
160 170 180 190 200
EKRDILVKHL IPQAVQLHTE RLKVQQVQGK WKVTDMVGDI CGDFKVPQAH
210 220 230 240 250
ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV GVINIPAANI
260 270 280 290 300
ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN
310 320 330 340 350
SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA
360 370 380 390 400
AGYYTALTMA IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ
410 420 430 440 450
WPAMFCNESE DAIRCPTSRL SLGACGVTRH PGLPPYWQYF TDPSLAGVSA
460 470 480 490 500
FMDYCPVVVP YSDGSCTQRA SEAHASLLPF NVFSDAARCI DGAFRPKATD
510 520 530 540 550
GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR VELSTVSNAF
560 570 580 590 600
EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV

AL
Length:602
Mass (Da):63,953
Last modified:April 1, 1990 - v2
Checksum:i982EF3245D87C43E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1.
PIRiPL0221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1 .
PIRi PL0221.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LML X-ray 1.86 A 100-577 [» ]
ProteinModelPortali P08148.
SMRi P08148. Positions 100-574.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M08.001.

PTM databases

UniCarbKBi P08148.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P08148.
PMAP-CutDB P08148.

Family and domain databases

InterProi IPR001577. Peptidase_M8.
[Graphical view ]
PANTHERi PTHR10942. PTHR10942. 1 hit.
Pfami PF01457. Peptidase_M8. 1 hit.
[Graphical view ]
PRINTSi PR00782. LSHMANOLYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of the major surface antigen of leishmania."
    Button L.L., McMaster W.R.
    J. Exp. Med. 167:724-729(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 101-123.
  2. Button L.L., McMaster W.R.
    J. Exp. Med. 171:589-589(1990)
    Cited for: SEQUENCE REVISION.
  3. "Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease."
    Schneider P., Ferguson M.A.J., McConville M.J., Mehlert A., Homans S.W., Bordier C.
    J. Biol. Chem. 265:16955-16964(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT ASN-577.
  4. "Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit."
    McGwire B.S., Chang K.-P.
    J. Biol. Chem. 271:7903-7909(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-254; HIS-264; GLU-265; HIS-268; ASN-300; ASN-407; ASN-534 AND ASN-577.
  5. "A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces."
    Funk V.A., Thomas-Oates J.E., Kielland S.L., Bates P.A., Olafson R.W.
    Mol. Biochem. Parasitol. 84:33-48(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-300 AND ASN-407.
  6. "Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major."
    Schlagenhauf E., Etges R., Metcalf P.
    Proteins 22:58-66(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-300; ASN-407 AND ASN-534.
  7. "The crystal structure of the Leishmania major surface proteinase leishmanolysin."
    Schlagenhauf E., Etges R., Metcalf P.
    Structure 6:1035-1046(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).

Entry informationi

Entry nameiGP63_LEIMA
AccessioniPrimary (citable) accession number: P08148
Secondary accession number(s): P15906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3